Structure-function analysis with a series of N-sulfonyloxy β-lactam molecules as inhibitors of β-lactamases is reported. The best of these compounds acylate the active site of the class A TEM-1 β-lactamase from Escherichia coli rapidly, and resist deacylation. Whereas acylation of the active site of the class C β-lactamase from Enterobacter cloacae was not seen, these compounds function as competitive inhibitors of this enzyme.
